Effect of Carnosine, Anserine and Other Endogenous Skeletal Peptides on the Activity of Porcine Muscle Alanyl and Arginyl Aminopeptidases

Abstract

The effect of endogenous dipeptides (carnosine and anserine) and peptidic fractions from meat extracts on aminopeptidase activity, alanyl and arginyl aminopeptidases purified from porcine skeletal muscle, was studied. Carnosine inhibited the activity ofporcine arginyl aminopeptidase (RAP); the inhibition being stronger with the purijied form of the enzyme than in the muscle extract. The RAP inhibition was competitive. One of the peptidic fractions isolated from meat extracts inhibited RAP activity but the degree of inhibition depended on the extent of purijcation. The major aminopeptidase present in muscle, alanyl aminopeptidase (AAP), was neither inhibited by natural dipeptides nor any of the peptidic fractions. The study of meat inhibitory peptides provides a better understanding of the action of proteolytic enzymes during meat processing.'Author for correspondence, Ph: 34 (96) 3900022, Fax: 34 (96) 3636301,

Intense Degradation of Myosin Light Chain Isoforms in Spanish Dry-Cured Ham

“…Aminopeptidase activity has been detected in meat products even after >8 months of processing, suggesting that these enzymes are involved in the later stages of protein degradation. Many factors, such as curing agent or the presence of other peptides, can modulate the activity of these enzymes. , …”

“…Many factors, such as curing agent or the presence of other peptides, can modulate the activity of these enzymes. 34,35 According to Toldr a et al, 33 alanyl and arginyl aminopeptidases, which show good stability during dry-cured processing and act at optimal neutral pH, appear to be the main contributors to the generation of free amino acids during the processing of dry-cured ham. Alanyl aminopeptidase (AAP, EC 3.4.11.14) is considered to be the major aminopeptidase in skeletal muscle with a broad range of specificity.…”

Model Studies on the Efficacy of Protein Homogenates from Raw Pork Muscle and Dry-Cured Ham in Binding Selected Flavor Compounds

“…In this sense, the interaction of proteins with volatile compounds significantly changes their headspace (HS) concentration and this interaction has been studied for vegetable proteins such as soy proteins (3)(4)(5) and pea proteins (6) as well as for animal proteins such as β-lactoglobulin (7)(8)(9), bovine serum albumin (10), and fish actomyosin (11). Furthermore, small components from muscle tissues such as dipeptides carnosine and anserine have been used in interaction studies (12,13).…”

Effect of high-pressure processing and chemical composition on lipid oxidation, aminopeptidase activity and free amino acids of Serrano dry-cured ham

“…Extracts were prepared following the method described by Gianelli, Flores, Moya, Aristoy, and Toldrá (2000). Representative ham samples without subcutaneous fat (10 g) were homogenized on ice with 50 ml of 50 mM phosphate buffer pH 7.5, containing 5 mM egtazic acid using an Ultraturrax T18 apparatus (3 × 10 s strokes).…”